about
peptidyl-tyrosine dephosphorylationpeptidyl-threonine dephosphorylationpeptidyl-serine dephosphorylationregulation of translational initiation by eIF2 alpha dephosphorylationhistone dephosphorylationdephosphorylation of RNA polymerase II C-terminal domainpeptidyl-histidine dephosphorylationpeptidyl-N-phospho-arginine dephosphorylation
P279
B cell leukemia/lymphoma 2Phosphatase and tensin homologLymphocyte protein tyrosine kinaseProtein tyrosine phosphatase, non-receptor type 11Pyruvate dehyrogenase phosphatase catalytic subunit 1Protein phosphatase 3 catalytic subunit gammaProtein tyrosine phosphatase non-receptor type 6Pyridoxal phosphataseProtein tyrosine phosphatase receptor type AProtein tyrosine phosphatase non-receptor type 4Protein tyrosine phosphatase non-receptor type 3Protein tyrosine phosphatase non-receptor type 21Protein phosphatase 6 catalytic subunitTGF-beta activated kinase 1 (MAP3K7) binding protein 1Protein tyrosine phosphatase non-receptor type 9Putative protein FAM220BPProtein tyrosine phosphatase receptor type TDual specificity phosphatase 11Dual specificity phosphatase 14Dual specificity phosphatase 3Dual specificity phosphatase 2Dual specificity phosphatase 4Dual specificity phosphatase 8Dual specificity phosphatase 5Dual specificity phosphatase 6Dual specificity phosphatase 7Serine/threonine/tyrosine interacting like 2Dual specificity phosphatase 29Dual specificity phosphatase 18Dual specificity phosphatase 19Dual specificity phosphatase 9Dual specificity phosphatase 23Dual specificity phosphatase 16Dual specificity phosphatase 15Dual specificity phosphatase 21Dual specificity phosphatase 22Dual specificity phosphatase 10Inorganic pyrophosphatase 2Protein tyrosine phosphatase receptor type MCalcineurin like phosphoesterase domain containing 1
P682
The nucleotide sequence of the cDNA encoding the human lung protein phosphatase 2A alpha catalytic subunitThe nucleotide sequence of the cDNA encoding the human lung protein phosphatase 2A beta catalytic subunitPhosphoinositide 3-kinase-mediated activation of cofilin phosphatase Slingshot and its role for insulin-induced membrane protrusionMolecular cloning of the human homolog of a striatum-enriched phosphatase (STEP) gene and chromosomal mapping of the human and murine lociIdentification, cloning, and expression of a cytosolic megakaryocyte protein-tyrosine-phosphatase with sequence homology to cytoskeletal protein 4.1Identification of a variant form of tyrosine phosphatase LYPSrc kinase associates with a member of a distinct subfamily of protein-tyrosine phosphatases containing an ezrin-like domainThe LAR/PTP delta/PTP sigma subfamily of transmembrane protein-tyrosine-phosphatases: multiple human LAR, PTP delta, and PTP sigma isoforms are expressed in a tissue-specific manner and associate with the LAR-interacting protein LIP.1cDNA cloning and characterization of a novel receptor-type protein tyrosine phosphatase expressed predominantly in the brainCharacterization of the myotubularin dual specificity phosphatase gene family from yeast to humanStructure of the 55-kDa regulatory subunit of protein phosphatase 2A: evidence for a neuronal-specific isoformPez: a novel human cDNA encoding protein tyrosine phosphatase- and ezrin-like domainsA novel human serine-threonine phosphatase related to the Drosophila retinal degeneration C (rdgC) gene is selectively expressed in sensory neurons of neural crest originMolecular cloning of a full-length cDNA encoding the catalytic subunit of human calmodulin-dependent protein phosphatase (calcineurin A alpha)Identification and characterization of a conserved family of protein serine/threonine phosphatases homologous to Drosophila retinal degeneration CA novel human protein serine/threonine phosphatase, which possesses four tetratricopeptide repeat motifs and localizes to the nucleusP-TEN, the tumor suppressor from human chromosome 10q23, is a dual-specificity phosphataseCloning and characterization of islet cell antigen-related protein-tyrosine phosphatase (PTP), a novel receptor-like PTP and autoantigen in insulin-dependent diabetesAssociation of SET domain and myotubularin-related proteins modulates growth controlCharacterization of the PEST family protein tyrosine phosphatase BDP1A family of putative tumor suppressors is structurally and functionally conserved in humans and yeastPP2C gamma: a human protein phosphatase with a unique acidic domainUBLCP1 is a 26S proteasome phosphatase that regulates nuclear proteasome activityNuclear tau, a key player in neuronal DNA protection.Reversion-induced LIM interaction with Src reveals a novel Src inactivation cycleOverexpression of PP1-NIPP1 limits the capacity of cells to repair DNA double-strand breaks
P921
Q14878357-0EFCCBE2-2C45-4184-81DA-ADF24007FFB5Q14912711-BCBED873-245D-480C-A927-446ACB794DE5Q21112033-61CCC79D-285C-49BE-BADD-0A039EC7234AQ21114210-17D5E0ED-D03E-41CE-8793-87B6FE9E8954Q21114414-9E2AB205-EE43-44CF-95A0-30AF73C89534Q21120510-4F154518-2286-4D01-ACF1-D13949950FF3Q21121935-55D971F2-1CB1-427A-9803-8DED1CD70FB7Q22284247-F8AA5BF3-67D4-416A-96E3-9F5CFA8A0601
P279
Q14863583-695ACF3E-93C2-46CA-A05D-729351610BCEQ14878408-D0C02C67-E8D5-4515-8A97-11C8D14B3A07Q14885208-DE78046D-6D6C-4DA3-805D-E3F14FEB2016Q14905498-F238706F-F144-4E48-BCBA-A13D6E74A646Q14912718-1FBD940F-0A5B-44E5-8BC4-5793143125B8Q14912718-865BEFDF-85BC-45A9-B7A9-F96EA4DDC872Q21097390-1B0B20A0-5D7E-446D-8270-4737112CEBDFQ21100543-9050EBDA-6679-435D-89C7-8BAF49A769ADQ21102052-2A79376E-4414-4397-A2FC-D1CB1FDAB486Q21102052-3702349C-1CA4-45D2-866A-9A5B3BD80744Q21102434-4C2689CD-3D75-4952-84F9-A9ABA49A52D1Q21102434-A3BEB779-2768-4AA1-AB2A-B9D3F7B3204FQ21102512-C2916DCF-01A3-4B89-BC0A-4C1819D332F9Q21105040-CDB197E4-489B-47E7-8376-E3FA1C737B1FQ21105085-6B5D3A96-9DE4-450A-94C6-94A7142EB92EQ21105132-33BD265C-3FE3-4A9A-8793-19738BBE8292Q21105132-7A9869C9-3D7C-4B93-9DFB-4651A0573EE7Q21105264-FDD1C1EF-584C-4F53-89AC-9DA17E611D5DQ21105307-62235BED-74FA-4EA0-BE0E-2A7CA1087BD8Q21105307-7172068B-9076-4971-A2E1-EB07A53CF6A5Q21106008-7B2BC524-22D0-49FB-B6F7-67FC51055575Q21106221-04C32516-04B5-4ECF-AC92-986EA1AC49EEQ21106221-A79A3E93-0C46-4EF1-AADF-F76707CDAED1Q21107134-C2D84B3A-55ED-46F0-9E0C-45BC4D21AFA4Q21107137-F60A03FF-ED35-4729-8742-403103B55DF8Q21107149-83CCC77F-1B9A-48EE-B9A9-307EDE658AABQ21107151-B5D02E4A-7E54-4417-A763-CCF421ABE87FQ21107153-E86711CB-BD03-4ACC-8778-6B12B6EFA766Q21107155-519DD370-F854-4468-BF0E-F377BE9D81AEQ21107155-91639308-A48B-406F-A9E7-5BFAF810A049Q21107157-42E55829-9145-457F-96C7-53FA7E861E8AQ21107163-3B0C5DD9-316C-43A6-ADB1-1E0A8670E2CBQ21107163-CFFDFDC7-5ACE-41B7-AE50-8C6089D47085Q21107180-10EA7E90-9CA5-4D2F-B810-4BC7891D554BQ21107180-898EE6BE-BD3B-45AA-A5FC-ED31EBD3D843Q21107182-8832A53F-483C-48BF-8E96-B4B1FF7975A5Q21107183-25E689BC-0637-46CB-9F23-456516610C37Q21107187-2F786E79-8DE7-45BC-86C5-1778376468A8Q21107190-5154E4F6-FB87-4378-AFE5-F0AB46FD2440Q21107197-68FD8547-1340-4DE1-9F9E-4308AF1E4939
P682
description
The process of removing one or more phosphoric residues from a protein.
@en
biologisch proces
@nl
name
protein dephosphorylation
@en
proteindefosforylering
@nn
type
label
protein dephosphorylation
@en
proteindefosforylering
@nn
altLabel
GO:0006470
@en
protein amino acid dephosphorylation
@en
prefLabel
protein dephosphorylation
@en
proteindefosforylering
@nn
P2888
P686
GO:0006470